ID   NLTP4_LENCU             Reviewed;         110 AA.
AC   A0AT33; P84255;
DT   15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   28-NOV-2006, sequence version 1.
DT   25-MAY-2022, entry version 47.
DE   RecName: Full=Non-specific lipid-transfer protein 4;
DE            Short=LTP4;
DE   Contains:
DE     RecName: Full=Non-specific lipid-transfer protein 8;
DE              Short=LTP8;
DE   Flags: Precursor; Fragment;
OS   Lens culinaris (Lentil) (Cicer lens).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; Hologalegina; IRL clade; Fabeae; Lens.
OX   NCBI_TaxID=3864;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 18-39, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Seed, and Seedling;
RX   PubMed=17511608; DOI=10.1134/s0006297907040104;
RA   Finkina E.I., Balandin S.V., Serebryakova M.V., Potapenko N.A.,
RA   Tagaev A.A., Ovchinnikova T.V.;
RT   "Purification and primary structure of novel lipid transfer proteins from
RT   germinated lentil (Lens culinaris) seeds.";
RL   Biochemistry (Mosc.) 72:430-438(2007).
CC   -!- FUNCTION: Plant non-specific lipid-transfer proteins transfer
CC       phospholipids as well as galactolipids across membranes. May play a
CC       role in wax or cutin deposition in the cell walls of expanding
CC       epidermal cells and certain secretory tissues.
CC   -!- MASS SPECTROMETRY: [Non-specific lipid-transfer protein 4]:
CC       Mass=9269.1; Method=MALDI; Note=LTP4.;
CC       Evidence={ECO:0000269|PubMed:17511608};
CC   -!- MASS SPECTROMETRY: [Non-specific lipid-transfer protein 8]:
CC       Mass=9121.9; Method=MALDI; Note=LTP8.;
CC       Evidence={ECO:0000269|PubMed:17511608};
CC   -!- SIMILARITY: Belongs to the plant LTP family. {ECO:0000255}.
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DR   EMBL; AY793558; AAX35811.1; -; mRNA.
DR   AlphaFoldDB; A0AT33; -.
DR   BMRB; A0AT33; -.
DR   SMR; A0AT33; -.
DR   Allergome; 8712; Len c 3.
DR   GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR   GO; GO:0006869; P:lipid transport; IEA:InterPro.
DR   Gene3D; 1.10.110.10; -; 1.
DR   InterPro; IPR036312; Bifun_inhib/LTP/seed_sf.
DR   InterPro; IPR016140; Bifunc_inhib/LTP/seed_store.
DR   InterPro; IPR000528; Plant_nsLTP.
DR   PANTHER; PTHR33076; PTHR33076; 1.
DR   Pfam; PF00234; Tryp_alpha_amyl; 1.
DR   PRINTS; PR00382; LIPIDTRNSFER.
DR   SMART; SM00499; AAI; 1.
DR   SUPFAM; SSF47699; SSF47699; 1.
DR   PROSITE; PS00597; PLANT_LTP; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; Lipid-binding; Signal;
KW   Transport.
FT   SIGNAL          <1..17
FT                   /evidence="ECO:0000269|PubMed:17511608"
FT   CHAIN           18..110
FT                   /note="Non-specific lipid-transfer protein 4"
FT                   /id="PRO_5000147978"
FT   CHAIN           18..109
FT                   /note="Non-specific lipid-transfer protein 8"
FT                   /id="PRO_0000287337"
FT   DISULFID        21..68
FT                   /evidence="ECO:0000250|UniProtKB:P23096"
FT   DISULFID        31..45
FT                   /evidence="ECO:0000250|UniProtKB:P23096"
FT   DISULFID        46..91
FT                   /evidence="ECO:0000250|UniProtKB:P23096"
FT   DISULFID        66..105
FT                   /evidence="ECO:0000250|UniProtKB:P23096"
FT   NON_TER         1
FT                   /evidence="ECO:0000312|EMBL:AAX35811.1"
SQ   SEQUENCE   110 AA;  11025 MW;  1ED2371DECF0888B CRC64;
     CVVLVMCMVV IAPMAEGAIS CGAVTSDLSP CLTYLTGGPG PSPQCCGGVK KLLAAANTTP
     DRQAACNCLK SAAGSITKLN TNNAAALPGK CGVNIPYKIS TSTNCNTVKF